4.8 Article

Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 131, Issue 18, Pages 6316-+

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ja8092604

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Funding

  1. National Institutes of Health [IPOIAG027818]

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A beta 40 and A beta 42 are peptides that adopt similar random-coil structures in solution. A beta 42, however, is significantly more neurotoxic than A beta 40 and forms amyloid fibrils much more rapidly than A beta 40. Here, mass spectrometry and ion mobility spectrometry are used to investigate a mixture of A beta 40 and A beta 42. The mass spectrum for the mixed solution shows the presence of a heterooligomer composed of equal parts of A beta 40 and A beta 42. Ion mobility results indicate that this mixed species comprises an oligomer distribution extending to tetramers. A beta 40 atone produces such a distribution, whereas A beta 42 alone produces oligomers as large as dodecamers. This indicates that A beta 40 inhibits A beta 42 oligomerization.

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